Using process of refolding the protein to obtain recombinant human interleukin-1 receptor antagonist.
- Author:
Shugang LI
1
;
Xiaoyan DENG
;
Hong ZHAO
;
Xiudong HUANG
;
Tinghe YU
;
Yong CHENG
;
Guoping DAN
Author Information
1. College of Bioengineering of Chongqing University, Chongqing 400044, China.
- Publication Type:Journal Article
- MeSH:
Escherichia coli;
genetics;
metabolism;
Humans;
Inclusion Bodies;
metabolism;
Interleukin 1 Receptor Antagonist Protein;
biosynthesis;
genetics;
Protein Folding;
Recombinant Proteins;
biosynthesis;
genetics;
isolation & purification
- From:
Journal of Biomedical Engineering
2007;24(5):1128-1132
- CountryChina
- Language:Chinese
-
Abstract:
Recombinant human interleukin-1 receptor antagonist was expressed in E. coli as an insoluble inclusion body. The inclusion body was dissolved in the 8 M urea and then the solution was diluted untill the concentration of urea became 2 M. By ion exchange chromatography the protein in the solution of 2 M urea was refolded and purified. At last the purity of product is more than 95% and its bioactivity is more than 1 x 10(5) IU/mg while it has little endotoxin. Western-Blotting also indicates that recombinant protein can react with antibodies against anti-hIL-1ra.
